Anti-DARS Antibody, Rabbit Polyclonal sinobiological 14278-RP01

$143.00
In stock
SKU
14278-RP01
Catalog No.SizePrice (USD)
14278-RP01-100100 µL$147.96
14278-RP01-200200 µL$251.64
14278-RP01-400400 µL$355.32

General Information

Product nameAnti-DARS Antibody, Rabbit Polyclonal
Validated applicationsELISA (FAQ Protocol)
Species reactivityReacts with: Human
SpecificityHuman DARS
ImmunogenRecombinant Human DARS protein (Catalog#14278-H07E)
PreparationProduced in rabbits immunized with purified, recombinant Human DARS (rh DARS; Catalog#14278-H07E; P14868; Met1-Pro501). Total IgG was purified by Protein A affinity chromatography.
SourcePolyclonal Rabbit IgG
PurificationProtein A
Formulation0.2 μm filtered solution in PBS
ConjugateUnconjugated
FormLiquid
ShippingThis antibody is shipped as liquid solution at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
StorageThis antibody can be stored at 2℃-8℃ for one month without detectable loss of activity. Antibody products are stable for twelve months from date of receipt when stored at -20℃ to -80℃. Preservative-Free. Avoid repeated freeze-thaw cycles.

Background Information

Full Nameaspartyl-tRNA synthetase
DescriptionAspartate tRNA ligase 1, also known as DARS, is part of a multienzyme complex of aminoacyl-tRNA synthetases. It belongs to the class-II aminoacyl-tRNA synthetase family. DARS charges its cognate tRNA with aspartate during protein biosynthesis. DARS catalyzes the specific attachment of an amino acid to its cognate tRNA in a 2 step reaction: the amino acid(AA) is first activated by ATP to form AA-AMP and then transferred to the acceptor end of the tRNA.
References
  1. Escalante C, et al. (1993) Expression of human aspartyl-tRNA synthetase in Escherichia coli. Functional analysis of the N-terminal putative amphiphilic helix. J Biol Chem. 268(8): 6014-23.
  2. Maruyama K, et al. (1994) Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides. Gene. 138(1-2):171-4.
  3. Reed VS, et al. (1995) Mechanisms of the transfer of aminoacyl-tRNA from aminoacyl-tRNA synthetase to the elongation factor 1 alpha. J Biol Chem. 269(52):32932-6.

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